Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions.
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Nascent β-Hairpin Formation of a Natively Unfolded Peptide Reveals the Role of Hydrophobic Contacts.The pKa Cooperative: a collaborative effort to advance structure-based calculations of pKa values and electrostatic effects in proteins.Interconnection of salt-induced hydrophobic compaction and secondary structure formation depends on solution conditions: revisiting early events of protein folding at single molecule resolution.Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.Effect of surfactant hydrophobicity on the pathway for unfolding of ubiquitin.Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Intrinsically disordered inhibitor of glutamine synthetase is a functional protein with random-coil-like pKa values.
P2860
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P2860
Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh
2011年學術文章
@zh-hant
name
Analysis of electrostatic inte ...... of L9 under native conditions.
@en
Analysis of electrostatic inte ...... of L9 under native conditions.
@nl
type
label
Analysis of electrostatic inte ...... of L9 under native conditions.
@en
Analysis of electrostatic inte ...... of L9 under native conditions.
@nl
prefLabel
Analysis of electrostatic inte ...... of L9 under native conditions.
@en
Analysis of electrostatic inte ...... of L9 under native conditions.
@nl
P2860
P356
P1433
P1476
Analysis of electrostatic inte ...... of L9 under native conditions.
@en
P2093
Wenli Meng
P2860
P304
P356
10.1002/PROT.23145
P407
P577
2011-09-13T00:00:00Z